Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

<i>d</i>-Band Engineering of Layered (Fe<sub>1-<i>x</i></sub>Ni<i><sub>x</sub></i>)<sub>3</sub>GaTe<sub>2</sub> for Enhanced Alkaline Hydrogen Evolution by Ni-Substitutional Doping.

Nanomaterials (Basel, Switzerland)·2026
Same author

Epidemiological characteristics of human parainfluenza virus infection in hospitalized children: a single-center study.

Frontiers in public health·2026
Same author

Classification with Missing Data - A <i>NIFty</i> Pipeline for Single-Cell Proteomics.

bioRxiv : the preprint server for biology·2026
Same author

A comparative analysis of CFD and LBM for investigating the effects of endothelial glycocalyx on the bifurcating blood flow.

Microvascular research·2026
Same author

Colloidal Structure Engineering of Perovskite Precursor for Efficient Pure Blue LEDs with High Chlorine Content.

ACS applied materials & interfaces·2026
Same author

Integrated GRM-based efficient multi-performance prediction method for reconfigurable Fabry-Perot antennas.

Scientific reports·2026

Related Experiment Video

Updated: Jul 6, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

A multidimensional chromatography technology for in-depth phosphoproteome analysis.

Claudio P Albuquerque1, Marcus B Smolka, Samuel H Payne

  • 1Ludwig Institute for Cancer Research, Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California 92093, USA.

Molecular & Cellular Proteomics : MCP
|April 15, 2008
PubMed
Summary

This study introduces a new multidimensional chromatography technique for deep phosphoproteome analysis. The method effectively identifies low-abundance phosphoproteins, advancing cellular signaling research.

More Related Videos

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
09:16

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

Related Experiment Videos

Last Updated: Jul 6, 2026

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification
10:37

Deep Proteome Profiling by Isobaric Labeling, Extensive Liquid Chromatography, Mass Spectrometry, and Software-assisted Quantification

Published on: November 15, 2017

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues
09:16

A Spin-Tip Enrichment Strategy for Simultaneous Analysis of N-Glycopeptides and Phosphopeptides from Human Pancreatic Tissues

Published on: May 4, 2022

Area of Science:

  • Biochemistry
  • Proteomics
  • Cellular Biology

Background:

  • Protein phosphorylation is a critical post-translational modification regulating cellular processes.
  • Global phosphorylation analysis aids in studying signaling pathways and kinase targets.
  • Analyzing low-abundance phosphoproteins requires advanced separation techniques due to phosphoproteome complexity.

Purpose of the Study:

  • To develop and validate a multidimensional chromatography technology for enhanced phosphopeptide purification and fractionation.
  • To enable in-depth mapping of low-abundance protein phosphorylation.
  • To improve the identification of phosphoproteins in complex biological samples.

Main Methods:

  • Development of a multidimensional chromatography system combining Immobilized Metal Affinity Chromatography (IMAC), hydrophilic interaction chromatography (HILIC), and reverse-phase Liquid Chromatography (LC).
  • Application of the technology to yeast (Saccharomyces cerevisiae) samples subjected to DNA damage.
  • Utilized tandem mass spectrometry (MS/MS) for phosphopeptide identification.

Main Results:

  • Successfully identified 8,764 unique phosphopeptides from 2,278 phosphoproteins in yeast.
  • Demonstrated effective identification of low-abundance proteins, with approximately 50% of phosphorylation sites identified for Rad9 and Mrc1.
  • The technology proved suitable for comprehensive phosphoproteome studies.

Conclusions:

  • The developed multidimensional chromatography technology significantly enhances the depth and scope of phosphoproteome analysis.
  • This approach is effective for identifying low-abundance phosphoproteins and mapping phosphorylation sites.
  • The technology provides a powerful tool for dissecting cellular signaling pathways through in-depth phosphoproteomics.